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Protein

Flippase kinase 1

Gene

FPK1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Flippase activator that phosphorylates DFN1 and DFN2 and which is involved in the generation of phospholipid asymmetry in membranes by the inward translocation of phospholipids and in the retrieval pathway from early endosomes to the trans-Golgi network (TGN). Phosphorylates also the N-terminal half of YPK1. Involved in pheromone-response.3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Down-regulated by YKP1 phosphorylation. This effect is counteracted in the presence of mannosyl-inositolphosphorylceramide (MIPC).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei525 – 5251ATPPROSITE-ProRule annotation
Active sitei621 – 6211Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi502 – 5109ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein kinase activity Source: SGD
  • protein serine/threonine kinase activity Source: SGD

GO - Biological processi

  • lipid transport Source: UniProtKB-KW
  • positive regulation of phospholipid translocation Source: SGD
  • protein autophosphorylation Source: SGD
  • protein phosphorylation Source: SGD
  • response to pheromone involved in conjugation with cellular fusion Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33354-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Flippase kinase 1 (EC:2.7.11.1)
Gene namesi
Name:FPK1
Ordered Locus Names:YNR047W
ORF Names:N3449
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XIV

Organism-specific databases

CYGDiYNR047w.
EuPathDBiFungiDB:YNR047W.
SGDiS000005330. FPK1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • mating projection tip Source: SGD
  • plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 893893Flippase kinase 1PRO_0000086154Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei140 – 1401Phosphoserine2 Publications
Modified residuei144 – 1441Phosphoserine1 Publication
Modified residuei171 – 1711Phosphoserine1 Publication
Modified residuei175 – 1751Phosphoserine1 Publication
Modified residuei185 – 1851Phosphoserine1 Publication
Modified residuei300 – 3001Phosphoserine2 Publications
Modified residuei414 – 4141Phosphoserine3 Publications
Modified residuei462 – 4621Phosphoserine2 Publications

Post-translational modificationi

The N-terminal non-catalytic domain is phosphorylated by YPK1.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53739.
PaxDbiP53739.
PRIDEiP53739.

Interactioni

Protein-protein interaction databases

BioGridi35872. 79 interactions.
DIPiDIP-6427N.
IntActiP53739. 6 interactions.
MINTiMINT-601192.

Structurei

3D structure databases

ProteinModelPortaliP53739.
SMRiP53739. Positions 420-854.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini496 – 777282Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini778 – 86184AGC-kinase C-terminalAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. KIN82 subfamily.PROSITE-ProRule annotation
Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00530000063286.
InParanoidiP53739.
KOiK08286.
OMAiGKIAYTP.
OrthoDBiEOG7R2BT5.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR011993. PH-like_dom.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53739-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGHHHEHEQ ERDHEQEHEH DSLQRPTTGS ERTRSISFSK LLTRSWKRNA
60 70 80 90 100
SSSNNMSVSS VNLYSDPENS RESDHNNSGS EGQSSRFSKL KSMFQSGNSS
110 120 130 140 150
KNASAHNSSQ SSLEGDSASS SSKLRYVKPM TSVANASPAS PPLSPTIPET
160 170 180 190 200
DVLQTPKMVH IDQHEHEREH SNCGSPIMLS SSSFSPTVAR TGTGRRRSPS
210 220 230 240 250
TPIMPSQNSN NSSSTSAIRP NNYRHHSGSQ GFSSNNPFRE RAGTVRSSNP
260 270 280 290 300
YFAYQGLPTH AMSSHDLDEG FQPYANGSGI HFLSTPTSKT NSLTNTKNLS
310 320 330 340 350
NLSLNEIKEN EEVQEFNNED FFFHDIPKDL SLKDTLNGSP SRGSSKSPTI
360 370 380 390 400
TQTFPSIIVG FDNEYEEDNN NDKHDEKEEQ QTTTDNKTRN LSPTKQNGKA
410 420 430 440 450
THPRIKIPLR RAASEPNGLQ LASATSPTSS SARKTSGSSN INDKIPGQSV
460 470 480 490 500
PPPNSFFPQE PSPKISDFPE PRRSRRLRTK SFSNKFQDIM VGPQSFEKIR
510 520 530 540 550
LLGQGDVGKV FLVREKKTNR VYALKVLSKD EMIKRNKIKR VLTEQEILAT
560 570 580 590 600
SNHPFIVTLY HSFQSEDYLY LCMEYCMGGE FFRALQTRKT KCICEDDARF
610 620 630 640 650
YASEVTAALE YLHLLGFIYR DLKPENILLH QSGHIMLSDF DLSIQAKDSK
660 670 680 690 700
VPVVKGSAQS TLVDTKICSD GFRTNSFVGT EEYIAPEVIR GNGHTAAVDW
710 720 730 740 750
WTLGILIYEM LFGFTPFKGD NTNETFTNIL KNEVSFPNNN EISRTCKDLI
760 770 780 790 800
KKLLTKNESK RLGCKMGAAD VKKHPFFKKV QWSLLRNQEP PLIPVLSEDG
810 820 830 840 850
YDFAKLSSNK KRQTSQDSHK HLDEQEKNMF EERVEYDDEV SEDDPFHDFN
860 870 880 890
SMSLMEQDNN SMIYGNTNSY GKIAYTPNSN RSRSNSHRTF FKR
Length:893
Mass (Da):100,546
Last modified:October 1, 1996 - v1
Checksum:i26AF74EE956F80DB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71662 Genomic DNA. Translation: CAA96328.1.
BK006947 Genomic DNA. Translation: DAA10588.1.
PIRiS63378.
RefSeqiNP_014445.1. NM_001183224.1.

Genome annotation databases

EnsemblFungiiYNR047W; YNR047W; YNR047W.
GeneIDi855783.
KEGGisce:YNR047W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71662 Genomic DNA. Translation: CAA96328.1.
BK006947 Genomic DNA. Translation: DAA10588.1.
PIRiS63378.
RefSeqiNP_014445.1. NM_001183224.1.

3D structure databases

ProteinModelPortaliP53739.
SMRiP53739. Positions 420-854.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35872. 79 interactions.
DIPiDIP-6427N.
IntActiP53739. 6 interactions.
MINTiMINT-601192.

Proteomic databases

MaxQBiP53739.
PaxDbiP53739.
PRIDEiP53739.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNR047W; YNR047W; YNR047W.
GeneIDi855783.
KEGGisce:YNR047W.

Organism-specific databases

CYGDiYNR047w.
EuPathDBiFungiDB:YNR047W.
SGDiS000005330. FPK1.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00530000063286.
InParanoidiP53739.
KOiK08286.
OMAiGKIAYTP.
OrthoDBiEOG7R2BT5.

Enzyme and pathway databases

BioCyciYEAST:G3O-33354-MONOMER.

Miscellaneous databases

NextBioi980256.
PROiP53739.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR011993. PH-like_dom.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Identification of novel pheromone-response regulators through systematic overexpression of 120 protein kinases in yeast."
    Burchett S.A., Scott A., Errede B., Dohlman H.G.
    J. Biol. Chem. 276:26472-26478(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  7. "Protein kinases Fpk1p and Fpk2p are novel regulators of phospholipid asymmetry."
    Nakano K., Yamamoto T., Kishimoto T., Noji T., Tanaka K.
    Mol. Biol. Cell 19:1783-1797(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-185; SER-300; SER-414 AND SER-462, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-144; SER-171; SER-175; SER-300; SER-414 AND SER-462, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "A protein kinase network regulates the function of aminophospholipid flippases."
    Roelants F.M., Baltz A.G., Trott A.E., Fereres S., Thorner J.
    Proc. Natl. Acad. Sci. U.S.A. 107:34-39(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION BY YPK1, ENZYME REGULATION.

Entry informationi

Entry nameiFPK1_YEAST
AccessioniPrimary (citable) accession number: P53739
Secondary accession number(s): D6W1M2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 22, 2015
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 752 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.